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Database: UniProt
Entry: A0A094E7K5_9PEZI
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ID   A0A094E7K5_9PEZI        Unreviewed;      1643 AA.
AC   A0A094E7K5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=DNA replication ATP-dependent helicase/nuclease {ECO:0000256|RuleBase:RU367041};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU367041};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU367041};
GN   ORFNames=V499_05432 {ECO:0000313|EMBL:KFY74554.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY74554.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY74554.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY74554.1,
RC   ECO:0000313|Proteomes:UP000029295};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key enzyme involved in DNA replication and DNA repair.
CC       Involved in Okazaki fragments processing by cleaving long flaps that
CC       escape FEN1: flaps that are longer than 27 nucleotides are coated by
CC       replication protein A complex (RPA), leading to recruit DNA2 which
CC       cleaves the flap until it is too short to bind RPA and becomes a
CC       substrate for FEN1. Also involved in 5'-end resection of DNA during
CC       double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
CC       {ECO:0000256|RuleBase:RU367041}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU367041};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC       Nucleus {ECO:0000256|RuleBase:RU367041}. Chromosome
CC       {ECO:0000256|RuleBase:RU367041}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007913, ECO:0000256|RuleBase:RU367041}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY74554.1}.
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DR   EMBL; JPKB01000869; KFY74554.1; -; Genomic_DNA.
DR   HOGENOM; CLU_001666_2_1_1; -.
DR   Proteomes; UP000029295; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR   CDD; cd18041; DEXXQc_DNA2; 1.
DR   CDD; cd22318; DNA2_N-like; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR022765; Dna2/Cas4_DUF83.
DR   InterPro; IPR026851; Dna2/JHS1_DEXXQ-box.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR048459; DNA2_Rift.
DR   InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR10887:SF433; DNA REPLICATION ATP-DEPENDENT HELICASE/NUCLEASE DNA2; 1.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF01930; Cas_Cas4; 1.
DR   Pfam; PF08696; Dna2; 1.
DR   Pfam; PF21123; Dna2_Rift; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU367041};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367041};
KW   Chromosome {ECO:0000256|RuleBase:RU367041};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367041};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367041};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU367041};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU367041};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU367041};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367041};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU367041};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU367041};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367041};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW   ECO:0000256|RuleBase:RU367041}; Nuclease {ECO:0000256|RuleBase:RU367041};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU367041};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367041}.
FT   DOMAIN          566..767
FT                   /note="DNA replication factor Dna2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08696"
FT   DOMAIN          774..878
FT                   /note="DUF83"
FT                   /evidence="ECO:0000259|Pfam:PF01930"
FT   DOMAIN          938..1030
FT                   /note="DNA2 rift barrel"
FT                   /evidence="ECO:0000259|Pfam:PF21123"
FT   DOMAIN          1132..1219
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          1237..1300
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          1308..1533
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1643 AA;  181445 MW;  6988595DED4F9C6F CRC64;
     MPLQKSFSDT NHSTKQRRPQ WQRNKTFHAP QNRYDVNPSE PARTKPPIPI SSATKSKLEV
     FQCNAQIKNR RSSIDMSGTG ANPLVLEEDK ENTPLKASEY GISPLSRKDF AKPSIETPAT
     PSSKLALPEL IGMMDVGSMA QLQLKTPDER VMWDQAINAV DNNSTSYVAP RRGGRKRPRS
     SSPMSSPGNI SSHFTANPEA GDIQQPGSHA AHAGPGLDLW SGYAIGADKF TPRGPPNPLF
     AHLMGNSSSP QSANVKNSAS REGTFKRSIS CGTQFPKRRK VGVFEDHTDV FTGPMKSALS
     KPSRVSELLD GIKVAAVSPD KLAFSSGPSS SSPIPRSKTW SERKEMHQAS PLGAKDRYVT
     TDAGIVEGEA PRLRLQPEER DDATVSQKSD STSSDYGDFD ADQFDESFLE VLESNQTSIQ
     TSQSPATAMY LDRRPINTQD SPAPAKKPSI MPPADAEEDD EFADSDEEMF AADFEEILSK
     YDTLPATADA GNQPALKQEE LAEGKGPDAK TVADIADSDD EYGDDLDDTD FAVAEASATQ
     AQALQNSASC FSNLSQKPRV LIVQVENTKE YRTIRLRDGW IETQVTEKAA VHVIGDFVSG
     QCVIDDSHSL LILHPDHLIS ATVVADSFGC TRRAVLQDRV KATSDSSAPL VYGTILHEIF
     QAAMMANRWD SPWLHDLIEK TATRHLEDLY TIKIQIPQAV EYLQSKMGEL QSWAEVFVTS
     KPHPEAIVKA GNGDTATMCV SKLLDVEEHV WSPMYGLKGN IDATVQVTMQ DAKSRRTLTV
     PFEVKTGKNA NASHRAQTAL YNLLLSDRYD IDIAYGILYY METSETIRIP AIRHELRHMI
     MQRNELACFV RERHAQLPPM LKKENLCGRC YAKTTCFIYH KLADDGDGET SGMKDKFDEV
     VKHLTPQHKE FFLKWDDLLT KEEKESLKFR RELWTMLSSE REKLGRCFSN VIIEPGSAYE
     EQDNPKINRF RYTLIRQDEA ANTSFLESQI TIGEPIVISD EKGHFALANG YVTHVRKHRI
     TVAVDRRLHN ARIRRPGFDE ANNQVFASIM EVAGEGSAPE STEGKITEAP VRYRLDKDEF
     SNGMATVRNN IIQLMADGPF MSRQLRSLIV DLEAPKFKSQ ATNYVLKDRE SINIDQRRAI
     DKVMSAQTYA LVLGMPGTGK TTTIAHIIRA LVSQGKSVLL ASYTHTAVDN ILLKLRDDKI
     PILRLGAAAK INAEVQEFAE LAAKPRSSFE ELGRLWHDTP VVATTCLGVN HAIFSERTFD
     YCIVDEASQI TLPVCLGPIR MARTFVLVGD HNQLPPLVQN EAARTGGLDV SLFKLLSDAH
     PAAVVNLEHQ YRMCAEVMAL SNELIYSGRL KCGTPEIAAR SISIPNMANL QTHHFSSSTM
     SRAGKTICAA PAKGQCWIRD LLDPATKACF VNTDTLVPRP REEAKGNRIV NPTEATICSQ
     LVQALLSVGV SGTEIGVMTH YRSQLALLKH NLRSHQEVEM HTCDRFQGRD KEVVVISLVR
     SNEAGGIGEL LRDWRRINVA FTRAKTKLLV VGSGSTLKGG EGGAEEMVGQ FVRLMERKAW
     VYDLPGGALD SHCFDDAATQ ASGSAAATPE KGGWKQLDLK AARMPGRAIG NENFKGPKKA
     VINERALFAG KPVLRDIMNE ARQ
//
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